CATH Classification

Domain Context

CATH Clusters

Superfamily Vaccinia Virus protein VP39
Functional Family Putative Histone-arginine methyltransferase CARM1

Enzyme Information

2.1.1.319
Type I protein arginine methyltransferase.
based on mapping to UniProt Q9WVG6
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.
-!- This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. -!- Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. -!- The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. -!- PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. -!- Cf. EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322. -!- Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.

UniProtKB Entries (2)

Q9WVG6
CARM1_MOUSE
Mus musculus
Histone-arginine methyltransferase CARM1
P11940
PABP1_HUMAN
Homo sapiens
Polyadenylate-binding protein 1

PDB Structure

PDB 5LGP
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
van Haren, M.J., Marechal, N., Troffer-Charlier, N., Cianciulli, A., Sbardella, G., Cavarelli, J., Martin, N.I.
Proc. Natl. Acad. Sci. U.S.A.